Variant position: 178 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 477 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human VASLAMDSLCRGVFAGNSRE LSIRSC-FPSLFQAEQTHRSIL
Mouse VASLAMDSLCRGVFAGNSRE LSIRSC-FPSLFQAEQTHRSI
Bovine VASLAMDSLCRGVFAGNSRE LSIRSC-FPSLFQAEQTHRSI
Slime mold MTKTFIEPTILGIYGGDYTN LSIKST-FKRAALLEPFGGLI
Baker's yeast ISNNMISALLRGIYGDDVSL LSAKRT-FKKIYYNELKHGSN
Fission yeast VTDRVMSAMINGIYAGDLND LSMHSSMFGFLAKIEKKYGNI
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 477 Protoporphyrinogen oxidase
166 – 166 L -> N. Decreases enzyme activity by 95%.
169 – 169 G -> A. Decreases enzyme activity by 64%.
Structural insight into human variegate porphyria disease.
Qin X.; Tan Y.; Wang L.; Wang Z.; Wang B.; Wen X.; Yang G.; Xi Z.; Shen Y.;
FASEB J. 25:653-664(2011)
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453; MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368;
Two new mutations (H106P and L178V) in the protoporphyrinogen oxidase gene in Argentinean patients with variegate porphyria.
De Siervi A.; Parera V.E.; del C Batlle A.M.; Rossetti M.V.;
Hum. Mutat. 16:532-532(2000)
Cited for: VARIANTS VP PRO-106 AND VAL-178;
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